5VE5
Crystal structure of persulfide dioxygenase rhodanese fusion protein with rhodanese domain inactivating mutation (C314S) from Burkholderia phytofirmans in complex with glutathione
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0050313 | molecular_function | sulfur dioxygenase activity |
A | 0070813 | biological_process | hydrogen sulfide metabolic process |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0050313 | molecular_function | sulfur dioxygenase activity |
B | 0070813 | biological_process | hydrogen sulfide metabolic process |
C | 0006749 | biological_process | glutathione metabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0050313 | molecular_function | sulfur dioxygenase activity |
C | 0070813 | biological_process | hydrogen sulfide metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue FE A 401 |
Chain | Residue |
A | HIS58 |
A | HIS114 |
A | ASP133 |
A | GSH402 |
A | HOH511 |
A | HOH545 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue GSH A 402 |
Chain | Residue |
A | GLY141 |
A | ARG142 |
A | TYR176 |
A | ARG193 |
A | LEU212 |
A | PRO215 |
A | LYS216 |
A | FE401 |
A | HIS114 |
A | ASP133 |
A | THR140 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue CL A 403 |
Chain | Residue |
A | ASP202 |
A | SER314 |
A | ARG315 |
A | ALA316 |
A | GLY317 |
A | GLY318 |
A | ARG319 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue IMD A 404 |
Chain | Residue |
A | PHE8 |
A | PHE8 |
A | TYR15 |
A | TYR15 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue PGE A 405 |
Chain | Residue |
A | PHE4 |
A | ARG5 |
A | GLN6 |
A | GLN6 |
A | TYR171 |
A | TYR171 |
A | THR180 |
A | THR180 |
A | VAL181 |
A | VAL181 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue FE B 401 |
Chain | Residue |
B | HIS58 |
B | HIS114 |
B | ASP133 |
B | GSH402 |
B | HOH503 |
B | HOH541 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GSH B 402 |
Chain | Residue |
B | HIS114 |
B | ASP133 |
B | LEU136 |
B | GLY141 |
B | ARG142 |
B | TYR176 |
B | FE401 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue CL B 403 |
Chain | Residue |
B | SER314 |
B | ARG315 |
B | ALA316 |
B | GLY318 |
B | ARG319 |
C | LEU198 |
C | ASP202 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue FE C 401 |
Chain | Residue |
C | HIS58 |
C | HIS114 |
C | ASP133 |
C | GSH402 |
C | HOH501 |
C | HOH526 |
site_id | AD1 |
Number of Residues | 11 |
Details | binding site for residue GSH C 402 |
Chain | Residue |
C | ASP62 |
C | THR140 |
C | GLY141 |
C | ARG142 |
C | TYR176 |
C | ARG193 |
C | PRO215 |
C | LYS216 |
C | FE401 |
C | HOH501 |
C | HOH526 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue CL C 403 |
Chain | Residue |
B | LEU198 |
B | ASP202 |
C | SER314 |
C | ARG315 |
C | ALA316 |
C | GLY318 |
C | ARG319 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue IMD C 404 |
Chain | Residue |
B | PHE8 |
B | TYR15 |
C | PHE8 |
C | TYR15 |